Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Conformational gating, dynamics and allostery in human monoacylglycerol lipase.

Scientific reports - 28 Oct 2020

Tyukhtenko Sergiy, Ma Xiaoyu, Rajarshi Girija, Karageorgos Ioannis, Anderson Kyle W, Hudgens Jeffrey W, Guo Jason J, Nasr Mahmoud L, Zvonok Nikolai, Vemuri Kiran, Wagner Gerhard, Makriyannis Alexandros

Abstract excerpt

Inhibition of human Monoacylglycerol Lipase (hMGL) offers a novel approach for treating neurological diseases. The design of inhibitors, targeting active-inactive conformational transitions of the enzyme, can be aided by understanding the interplay between structure and dynamics. Here, we report the effects of mutations within the catalytic triad on structure, conformational gating and dynamics of hMGL by...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Allosteric Regulation
Share to Catalysis

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Kinetics

Share to Magnetic Resonance Spectroscopy

Share to Molecular Dynamics Simulation

Share to Mutation, Missense

Share to Protein Conformation

Share to Structure-Activity Relationship

Source

Open in PubMed Open full text

Identifiers

PMID: 33116203
DOI: 10.1038/s41598-020-75497-5
PMCID: PMC7595040

Genes

HDX

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Conformational gating, dynamics and allostery in human monoacylglycerol lipase.PMID 33116203Read ↗

Covalent inhibitors of human monoacylglycerol lipase: ligand-assisted characterization of the catalytic site by mass spectrometry and mutational analysis.Semantic proximity Read ↗

Mutation of Cys242 of human monoacylglycerol lipase disrupts balanced hydrolysis of 1- and 2-monoacylglycerols and selectively impairs inhibitor potency.Semantic proximity Read ↗

Structure of product-bound SMG1 lipase: active site gating implications.Semantic proximity Read ↗

ASM Variants in the Spotlight: A Structure-Based Atlas for Unraveling Pathogenic Mechanisms in Lysosomal Acid SphingomyelinaseSemantic proximity Read ↗

The structure of monoacylglycerol lipase from Bacillus sp. H257 reveals unexpected conservation of the cap architecture between bacterial and human enzymesSemantic proximity Read ↗

Keys to Lipid Selection in Fatty Acid Amide Hydrolase Catalysis: Structural Flexibility, Gating Residues and Multiple Binding Pockets.Semantic proximity Read ↗

Endocannabinoid enzyme engineering: soluble human thio-monoacylglycerol lipase (sol-S-hMGL).Semantic proximity Read ↗

ASM variants in the spotlight: A structure-based atlas for unraveling pathogenic mechanisms in lysosomal acid sphingomyelinaseSemantic proximity Read ↗

The role of human monoacylglycerol lipase (hMAGL) binding pocket in breakup of unsaturated phospholipid membranes.Semantic proximity Read ↗

Crystal structure of human lysosomal acid lipase and its implications in cholesteryl ester storage disease.Semantic proximity Read ↗

Dynamic coupling of residues within proteins as a mechanistic foundation of many enigmatic pathogenic missense variants.Semantic proximity Read ↗

A distant angiogenin variant causes amyotrophic lateral sclerosis through loss-of-function mechanisms: Insights from long-timescale atomistic simulations and conformational dynamics.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.